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Extracellular phosphorylation in the parasite, Leishmania major
D S Lester1, T Hermoso, C L Jaffe
1Department of Membrane Research, MacArthur Center for Molecular Biology of Tropical Diseases, Weizmann Institute of Science, Rehovot, Israel.
Biochimica Et Biophysica Acta
|May 2, 1990
Summary
Researchers identified eleven phosphoproteins in Leishmania major using adenosine 5'[gamma-32P]-triphosphate (ATP). The parasite
Area of Science:
- Parasitology
- Biochemistry
- Molecular Biology
Background:
- Leishmania major is an important parasite causing leishmaniasis.
- Understanding parasite phosphorylation is crucial for host-parasite interaction studies.
Purpose of the Study:
- To investigate protein phosphorylation in Leishmania major.
- To characterize the protein kinase activity and identify phosphoproteins.
Main Methods:
- Labeling intact promastigotes and cell-free extracts with adenosine 5'[gamma-32P]-triphosphate (ATP).
- Analyzing phosphoprotein profiles and substrate specificity.
- Investigating the localization and properties of kinase activity.
Main Results:
- Identified eleven phosphoproteins in Leishmania major.
- Demonstrated unique kinase activity insensitive to common inhibitors, suggesting a novel class of kinases.
- Localized significant kinase activity to the cell membrane (ecto-kinase).
- Observed differential effects of cyclic AMP on phosphorylation.
- Found three serine-labeled phosphoproteins released into the medium.
Conclusions:
- Leishmania major possesses unique protein kinase(s), potentially a new class.
- An ecto-kinase activity and secreted phosphoproteins may be involved in host-parasite interactions.